8C4A

Structural and interactional insights into the glideosome-associated connector from Toxoplasma gondii

Summary for 8C4A

• Entry DOI: 10.2210/pdb8c4a/pdb
• Descriptor: Putative anonymous antigen-1 (2 entities in total)
• Functional Keywords: glideosome-associated connector (gac), toxoplasma gondii, structural protein
• Biological source: Toxoplasma gondii
• Total number of polymer chains: 1
• Total formula weight: 274375.75

Authors

Kumar, A.,Morgan, R.M.L.,Matthews, S.J. (deposition date: 2023-01-03, release date: 2023-07-19, Last modification date: 2024-11-06)

Primary citation

Kumar, A.,Vadas, O.,Dos Santos Pacheco, N.,Zhang, X.,Chao, K.,Darvill, N.,Rasmussen, H.O.,Xu, Y.,Lin, G.M.,Stylianou, F.A.,Pedersen, J.S.,Rouse, S.L.,Morgan, M.L.,Soldati-Favre, D.,Matthews, S.
Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii.
Elife, 12:-, 2023

PubMed Abstract: The phylum of Apicomplexa groups intracellular parasites that employ substrate-dependent gliding motility to invade host cells, egress from the infected cells, and cross biological barriers. The glideosome-associated connector (GAC) is a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesins and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. Here, we present the crystal structure of GAC and reveal a unique, supercoiled armadillo repeat region that adopts a closed ring conformation. Characterisation of the solution properties together with membrane and F-actin binding interfaces suggests that GAC adopts several conformations from closed to open and extended. A multi-conformational model for assembly and regulation of GAC within the glideosome is proposed.

PubMed: 37014051
DOI: 10.7554/eLife.86049

Experimental method

X-RAY DIFFRACTION (2.675 Å)